| Title : Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y - Jung_1995_Protein.Sci_4_2433 |
| Author(s) : Jung G , Ueno H , Hayashi R , Liao TH |
| Ref : Protein Science , 4 :2433 , 1995 |
|
Abstract :
The essential histidine residue of carboxypeptidase Y (CPY) was modified by a site-specific reagent, a chloromethylketone derivative of benzyloxycarbonyl-L-phenylalanine. The single modified histidine residue was converted to N tau-carboxy-methyl histidine (cmHis) upon performic acid oxidation. A peptide containing cmHis was isolated from the tryptic-thermolytic digest. Based on the amino acid composition and sequence analysis, the peptide is shown to be Val-Phe-Asp-Gly-Gly-cmHis-MetO2-Val-Pro, which was derived from CPY cleaved by trypsin at Arg 391 and thermolysin at Phe 401, and thus His 397 was modified. This histidine residue has been implicated previously by X-ray analysis to participate in the charge-relay system of CPY. |
| PubMedSearch : Jung_1995_Protein.Sci_4_2433 |
| PubMedID: 8563642 |
| Gene_locus related to this paper: yeast-cbpy1 |
| Gene_locus | yeast-cbpy1 |
Jung G, Ueno H, Hayashi R, Liao TH (1995)
Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y
Protein Science
4 :2433
Jung G, Ueno H, Hayashi R, Liao TH (1995)
Protein Science
4 :2433